The Role of Cullin-RING Ligases in Striated Muscle Development, Function, and Disease

• The well-orchestrated turnover of proteins in cross-striated muscles is one of the fundamental processes required for muscle cell function and survival. Dysfunction of the intricate protein degradation machinery is often associated with development of cardiac and skeletal muscle myopathies. Most muscle proteins are degraded by the ubiquitin-proteasome system (UPS). The UPS involves a number of enzymes, including E3-ligases, which tightly control which protein substrates are marked for degradation by the proteasome. Recent data reveal that E3-ligases of the cullin family play more diverse and crucial roles in cross striated muscles than previously anticipated. This review highlights some of the findings on the multifaceted functions of cullin-RING E3-ligases, their substrate adapters, muscle protein substrates, and regulatory proteins, such as the Cop9 signalosome, for the development of cross striated muscles, and their roles in the etiology of myopathies.

Ämnesord

MEDICIN OCH HÄLSOVETENSKAP  -- Klinisk medicin (hsv//swe)

MEDICAL AND HEALTH SCIENCES  -- Clinical Medicine (hsv//eng)

Nyckelord

cullin-RING ligase (CRL)

Nedd8

protein degradation

ubiquitin-proteasome system (UPS)

autophagy-lysosome system

striated

muscle development

striated muscle function

muscular dystrophy

cardiomyopathy

f-box protein

e3 ubiquitin ligases

nedd8-activating enzyme-inhibitor

transcription elongation-factor

disrupts glucose-homeostasis

tumor-suppressor protein

cop9 signalosome complex

skeletal-muscle

ankyrin-repeat

nemaline myopathy

Biochemistry & Molecular Biology

Chemistry

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